2.7.1.130	D138A	point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity	723650	
2.7.1.130	D138A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675, 738621	
2.7.1.130	D138N	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675, 738621	
2.7.1.130	D139A	point mutant of conserved residue, not directly involved in ADP or Mg2+ binding. About 0.1% of wild-type activity	723650	
2.7.1.130	D139A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675, 738621	
2.7.1.130	D139N	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675, 738621	
2.7.1.130	D260A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675	
2.7.1.130	D99A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675	
2.7.1.130	D99E	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675	
2.7.1.130	D99N	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675	
2.7.1.130	E100A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675, 738621	
2.7.1.130	E100D	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675	
2.7.1.130	E100Q	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675	
2.7.1.130	E172A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	738621	
2.7.1.130	G47A	about 43% of wild-type activity	723650	
2.7.1.130	G48A	about 1.8% of wild-type activity	723650	
2.7.1.130	G50A	about 0.1% of wild-type activity	723650	
2.7.1.130	H143A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	738621	
2.7.1.130	H261A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675, 738621	
2.7.1.130	K51A	about 0.1% of wild-type activity	723650	
2.7.1.130	K51A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675	
2.7.1.130	additional information	steady-state kinetic analysis of multiple point mutants of the lipid-binding pocket pinpoints critical residues involved in substrate binding, and construction of two N-terminal helix truncated forms of LpxK, one in which amino acids 2-12 are removed, DELTA12LpxK, and another in which amino acids 2-29 are removed, DELTA29LpxK	738621	
2.7.1.130	N43A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	738621	
2.7.1.130	Q142A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	738621	
2.7.1.130	R119A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	738621	
2.7.1.130	R171A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	738621	
2.7.1.130	R72A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	738621	
2.7.1.130	S49A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675	
2.7.1.130	S53A	about 9.9% of wild-type activity	723650	
2.7.1.130	S53A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675	
2.7.1.130	T52A	about 0.1% of wild-type activity	723650	
2.7.1.130	T52A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675	
2.7.1.130	Y74A	site-directed mutagenesis, the mutant shows altered activity compared to the wild-type enzyme	737675, 738621